Production and purification of the penicillin-binding protein 3 from Pseudomonas aeruginosa

León, Sandra Ruiloba de; Daniels, Kathy; Clarke, Anthony J.

doi:10.1016/j.pep.2010.05.005

Cited by 4 publications

(1 citation statement)

References 31 publications

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“…Class B PBPs have an N-terminal domain of unknown function and a C-terminal domain containing transpeptidase activity [17]. They are also HMW PBPs but are smaller in size compared to Class A PBPs [18]. Class C PBPs are LMW PBPs, usually having molecular weights below 50 kDa [19].…”

Section: Introductionmentioning

confidence: 99%

Structural Insights into the Penicillin-Binding Protein 4 (DacB) from Mycobacterium tuberculosis

Kang,

Kim

2024

IJMS

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Mycobacterium tuberculosis, a major cause of mortality from a single infectious agent, possesses a remarkable mycobacterial cell envelope. Penicillin-Binding Proteins (PBPs) are a family of bacterial enzymes involved in the biosynthesis of peptidoglycan. PBP4 (DacB) from M. tuberculosis (MtbPBP4) has been known to function as a carboxypeptidase, and the role and significance of carboxypeptidases as targets for anti-tuberculosis drugs or antibiotics have been extensively investigated over the past decade. However, their precise involvement remains incompletely understood. In this study, we employed predictive modeling and analyzed the three-dimensional structure of MtbPBP4. Interestingly, MtbPBP4 displayed a distinct domain structure compared to its homologs. Docking studies with meropenem verified the presence of active site residues conserved in PBPs. These findings establish a structural foundation for comprehending the molecular function of MtbPBP4 and offer a platform for the exploration of novel antibiotics.

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Section: Introductionmentioning

confidence: 99%

Structural Insights into the Penicillin-Binding Protein 4 (DacB) from Mycobacterium tuberculosis

Kang,

Kim

2024

IJMS

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Crystal structures of penicillin‐binding protein 3 in complexes with azlocillin and cefoperazone in both acylated and deacylated forms

et al. 2016

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Penicillin‐binding protein 3 (PBP3) from Pseudomonas aeruginosa is the molecular target of β‐lactam‐based antibiotics. Structures of PBP3 in complexes with azlocillin and cefoperazone, which are in clinical use for the treatment of pseudomonad infections, have been determined to 2.0 Å resolution. Together with data from other complexes, these structures identify a common set of residues involved in the binding of β‐lactams to PBP3. Comparison of wild‐type and an active site mutant (S294A) showed that increased thermal stability of PBP3 following azlocillin binding was entirely due to covalent binding to S294, whereas cefoperazone binding produces some increase in stability without the covalent link. Consistent with this, a third crystal structure was determined in which the hydrolysis product of cefoperazone was noncovalently bound in the active site of PBP3. This is the first structure of a complex between a penicillin‐binding protein and cephalosporic acid and may be important in the design of new noncovalent PBP3 inhibitors.

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Revealing extracellular protein profile and excavating spoilage-related proteases of Aeromonas salmonicida based on multi-omics investigation

Shao,

Dong,

Chen

et al. 2024

International Journal of Biological Macromolecules

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Production and purification of the penicillin-binding protein 3 from Pseudomonas aeruginosa

Cited by 4 publications

References 31 publications

Structural Insights into the Penicillin-Binding Protein 4 (DacB) from Mycobacterium tuberculosis

Structural Insights into the Penicillin-Binding Protein 4 (DacB) from Mycobacterium tuberculosis

Crystal structures of penicillin‐binding protein 3 in complexes with azlocillin and cefoperazone in both acylated and deacylated forms

Revealing extracellular protein profile and excavating spoilage-related proteases of Aeromonas salmonicida based on multi-omics investigation

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